C345C

The netrin (NTR) module is an about 130-residue domain found in the C-terminal parts of netrins, complement proteins C3, C4, and C5, secreted frizzled-related proteins, and type I procollagen C-proteinase enhancer proteins (PCOLCEs), as well as in the N-terminal parts of tissue inhibitors of metalloproteinases (TIMPs). The proteins harboring the NTR domain fulfill diverse biological roles ranging from axon guidance, regulation of Wnt signalling, to the control of the activity of metalloproteinases. The NTR domain can be found associated to other domains such as CUB, WAP, Kazal, Kunitz, Ig-like, laminin N-terminal, laminin-type EGF or frizzled. The NTR domain is implicated in inhibition of zinc metalloproteinases of the metzincin family [(PUBMED:10452607), (PUBMED:11274388)].

The NTR module is a basic domain containing six conserved cysteines, which are likely to form internal disulphide bonds, and several conserved blocks of hydrophobic residues (including an YLLLG-like motif). The NTR module consists of a beta-barrel with two terminal alpha-helices packed side by side against the face of the beta-barrel (see P16035) [(PUBMED:10452607)].

This entry includes most netrin modules, but excludes those found in TIMPs.

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with C345C domain which could be assigned to a KEGG orthologous group, and not all proteins containing C345C domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.